Lymphocyte antigen 96 precursor - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot Q9Y6Y9 (LY96_HUMAN)

Last modified February 9, 2010. Version 84. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Lymphocyte antigen 96
      Short name=Ly-96
Alternative name(s):
    Protein MD-2
    ESOP-1

Gene names

Name:	LY96
Synonyms:	ESOP1, MD2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	160 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Cooperates with TLR4 in the innate immune response to bacterial lipopolysaccharide (LPS), and with TLR2 in the response to cell wall components from Gram-positive and Gram-negative bacteria. Enhances TLR4-dependent activation of NF-kappa-B. Cells expressing both MD2 and TLR4, but not TLR4 alone, respond to LPS.
Subunit structure	Heterogeneous homopolymer formed from homodimers; disulfide-linked. Belongs to the lipopolysaccharide (LPS) receptor, a multi-protein complex containing at least CD14, LY96 and TLR4. Binds to the extracellular domains of TLR2 and TLR4. Ligand binding induces interaction with TLR4 and oligomerization of the complex. Ref.6 Ref.7 Ref.8 Ref.10
Subcellular location	Secreted › extracellular space.
Post-translational modification	N-glycosylated; high-mannose. Ref.7 Ref.10

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Ontologies

Keywords
Biological process	Immune response Inflammatory response
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	I-kappaB kinase/NF-kappaB cascade Inferred from Experiment. Source: Reactome cell surface receptor linked signal transduction Ref.1 Traceable author statement. Source: ProtInc cellular defense response Ref.1 Traceable author statement. Source: ProtInc detection of lipopolysaccharide Inferred from direct assay. Source: UniProtKB immune response Inferred from electronic annotation. Source: UniProtKB-KW inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell lipopolysaccharide receptor complex Inferred from direct assay. Source: UniProtKB plasma membrane Ref.1 Inferred from Experiment. Source: Reactome
Molecular function	coreceptor activity Ref.1 Traceable author statement. Source: ProtInc lipopolysaccharide receptor activity Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

Potential

Chain

19 – 160

142

Lymphocyte antigen 96

PRO_0000018619

Regions

Region

119 – 123

Interaction with lipopolysaccharide

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Ref.10

Glycosylation

114

N-linked (GlcNAc...) Ref.10

Disulfide bond

Disulfide bond

Disulfide bond

Natural variations

Natural variant

G → R: dbSNP rs6472812.

VAR_050030

Natural variant

157

P → S: dbSNP rs11466004.

VAR_024532

Experimental info

Mutagenesis

C → Y: Abolishes LPS-response. Ref.3

Secondary structure

160

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9Y6Y9-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 1E83AFF583636D7A
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FASTA

160

18,446

        10         20         30         40         50         60 
MLPFLFFSTL FSSIFTEAQK QYWVCNSSDA SISYTYCDKM QYPISINVNP CIELKGSKGL 

        70         80         90        100        110        120 
LHIFYIPRRD LKQLYFNLYI TVNTMNLPKR KEVICRGSDD DYSFCRALKG ETVNTTISFS 

       130        140        150        160 
FKGIKFSKGK YKCVVEAISG SPEEMLFCLE FVILHQPNSN

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4." Shimazu R., Akashi S., Ogata H., Nagai Y., Fukudome K., Miyake K., Kimoto M. J. Exp. Med. 189:1777-1782(1999) [PubMed: 10359581] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Uterus.
[2]	"ESOP-1, a secreted protein expressed in the hematopoietic, nervous, and reproductive systems of embryonic and adult mice." Kato K., Morrison A.M., Nakano T., Tashiro K., Honjo T. Blood 96:362-364(2000) [PubMed: 10891475] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Molecular genetic analysis of an endotoxin nonresponder mutant cell line. A point mutation in a conserved region of MD-2 abolishes endotoxin-induced signaling." Schromm A.B., Lien E., Henneke P., Chow J.C., Yoshimura A., Heine H., Latz E., Monks B.G., Schwartz D.A., Miyake K., Golenbock D.T. J. Exp. Med. 194:79-88(2001) [PubMed: 11435474] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF CYS-95.
[4]	"Natural selection in the TLR-related genes in the course of primate evolution." Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T., Kimura A. Immunogenetics 60:727-735(2008) [PubMed: 18810425] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[6]	"MD-2 enables Toll-like receptor 2 (TLR2)-mediated responses to lipopolysaccharide and enhances TLR2-mediated responses to Gram-positive and Gram-negative bacteria and their cell wall components." Dziarski R., Wang Q., Miyake K., Kirschning C.J., Gupta D. J. Immunol. 166:1938-1944(2001) [PubMed: 11160242] [Abstract] Cited for: INTERACTION WITH TLR2 AND TLR4.
[7]	"Secreted MD-2 is a large polymeric protein that efficiently confers lipopolysaccharide sensitivity to Toll-like receptor 4." Visintin A., Mazzoni A., Spitzer J.A., Segal D.M. Proc. Natl. Acad. Sci. U.S.A. 98:12156-12161(2001) [PubMed: 11593030] [Abstract] Cited for: DISULFIDE BONDS, GLYCOSYLATION.
[8]	"The role of disulfide bonds in the assembly and function of MD-2." Mullen G.E.D., Kennedy M.N., Visintin A., Mazzoni A., Leifer C.A., Davies D.R., Segal D.M. Proc. Natl. Acad. Sci. U.S.A. 100:3919-3924(2003) [PubMed: 12642668] [Abstract] Cited for: INTERCHAIN DISULFIDE BOND.
[9]	"Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran." Kim H.M., Park B.S., Kim J.-I., Kim S.E., Lee J., Oh S.C., Enkhbayar P., Matsushima N., Lee H., Yoo O.J., Lee J.-O. Cell 130:906-917(2007) [PubMed: 17803912] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 19-158 IN COMPLEX WITH TLR4 AND LIPOPOLYSACCHARIDE ANALOG.
[10]	"Crystal structures of human MD-2 and its complex with antiendotoxic lipid IVa." Ohto U., Fukase K., Miyake K., Satow Y. Science 316:1632-1634(2007) [PubMed: 17569869] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 17-160 IN COMPLEX WITH LIPID IV-A, DISULFIDE BONDS, GLYCOSYLATION AT ASN-26 AND ASN-114.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB018549 mRNA. Translation: BAA78717.1.
AF168121 mRNA. Translation: AAF89635.1.
AB446498 mRNA. Translation: BAG55275.1.
BC020690 mRNA. Translation: AAH20690.1.

IPI

IPI00022250.

RefSeq

NP_056179.2.

UniGene

Hs.660766

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1T2Z	model	-	A	19-160	[»]
2E56	X-ray	2.00	A	17-160	[»]
2E59	X-ray	2.21	A	17-160	[»]
2Z65	X-ray	2.70	C/D	19-158	[»]
3FXI	X-ray	3.10	C/D	19-160	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q9Y6Y9.

Proteomic databases

PRIDE

Q9Y6Y9.

Genome annotation databases

Ensembl

ENST00000284818; ENSP00000284818; ENSG00000154589; Homo sapiens. [Genome view]

GeneID

23643.

KEGG

hsa:23643.

UCSC

uc003yad.1. human.

Organism-specific databases

CTD

23643.

GeneCards

GC08P075066.

H-InvDB

HIX0007590.

HGNC

HGNC:17156. LY96.

MIM

605243. gene.

PharmGKB

PA134924906.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG20247.

HOGENOM

HBG125893.

HOVERGEN

Q9Y6Y9.

InParanoid

Q9Y6Y9.

Enzyme and pathway databases

Reactome

REACT_6900. Signaling in Immune system.
REACT_6968. Mal Cascade.

Gene expression databases

ArrayExpress

Q9Y6Y9.

Bgee

Q9Y6Y9.

CleanEx

HS_LY96.

Genevestigator

Q9Y6Y9.

GermOnline

ENSG00000154589. Homo sapiens.

Family and domain databases

InterPro

IPR003172. MD-2_lipid-recog.
[Graphical view]

Pfam

PF02221. E1_DerP2_DerF2. 1 hit.
[Graphical view]

SMART

SM00737. ML. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

46449.

SOURCE

Search...

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Entry information

Entry name

LY96_HUMAN

Accession

Primary (citable) accession number: Q9Y6Y9
Secondary accession number(s): B3Y6A5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 27, 2002
Last sequence update:	November 1, 1999
Last modified:	February 9, 2010
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Human chromosome 8: entries, gene names and cross-references to MIM

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references